Histochemical study of lectin binding sites in fourth and fifth instar gypsy moth larval midgut epithelium

Abstract

There is evidence that the gypsy moth, Lymantria dispar, midgut epithelial brush border membrane has membrane-bound glycoconjugates, such as BTR-270 and aminopeptidase N (APN), which function as high affinity binding sites (receptors) for the insecticidal proteins produced by Bacillus thuringiensis (Bt). As gypsy moth larvae become older, they become resistant to the entomocidal activity of Bt, suggesting there may be a change in the expression of these toxin-binding glycoconjugates in older larvae.

Parent Publication

• Proceedings, 21st U.S. Department of Agriculture interagency research forum on invasive species 2010

Citation

Valaitis, Algimantas P. 2011. Histochemical study of lectin binding sites in fourth and fifth instar gypsy moth larval midgut epithelium. In: McManus, Katherine A; Gottschalk, Kurt W., eds. 2010. Proceedings. 21st U.S. Department of Agriculture interagency research forum on invasive species 2010; 2010 January 12-15; Annapolis, MD. Gen. Tech. Rep. NRS-P-75. Newtown Square, PA: U.S. Department of Agriculture, Forest Service, Northern Research Station: 139.